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Reviewed, UniProtKB/Swiss-Prot P39929 (SNF7_YEAST)

Last modified November 24, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vacuolar-sorting protein SNF7
Alternative name(s):
    Vacuolar protein-sorting-associated protein 32
    DOA4-independent degradation protein 1
Gene names
Name: SNF7
Synonyms: DID1, VPS32
Ordered Locus Names: YLR025W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Appears to sequester MVB cargo. Recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles. Ref.3 Ref.4

Subunit structure

Self-associates. Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with VTA1; the interaction requires DID2. Interacts with BRO1. Ref.4 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm. Endosome membrane; Peripheral membrane protein.

Miscellaneous

Present with 3270 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the SNF7 family.

Caution

Was originally (Ref.1) thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Vacuolar-sorting protein SNF7
PRO_0000211446

Regions

Compositional bias68 – 714Poly-Lys
Compositional bias216 – 22813Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue721Phosphothreonine Ref.9 Ref.10 Ref.13
Modified residue1161Phosphothreonine Ref.13
Modified residue1191Phosphoserine Ref.10 Ref.13
Modified residue1931Phosphoserine Ref.13
Modified residue2041Phosphoserine Ref.13
Modified residue2131Phosphoserine Ref.11

Sequences

Sequence LengthMass (Da)Tools
P39929-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5241A18BB181F0C1

FASTA24026,987
        10         20         30         40         50         60 
MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE ARIFLTKGNK 

        70         80         90        100        110        120 
VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN LETMRAMQEG AKAMKTIHSG 

       130        140        150        160        170        180 
LDIDKVDETM DEIREQVELG DEISDAISRP LITGANEVDE DELDEELDML AQENANQETS 

       190        200        210        220        230        240 
KIVNNNVNAA PISENKVSLP SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae."
Tu J., Vallier L.G., Carlson M.
Genetics 135:17-23(1993) [PubMed: 8224817] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
J. Cell Sci. 114:2395-2404(2001) [PubMed: 11559748] [Abstract]
Cited for: FUNCTION.
[4]"Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting."
Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.
Dev. Cell 3:271-282(2002) [PubMed: 12194857] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS20, SUBCELLULAR LOCATION.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
Traffic 5:194-210(2004) [PubMed: 15086794] [Abstract]
Cited for: INTERACTION WITH BRO1.
[7]"Structural basis for endosomal targeting by the Bro1 domain."
Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H.
Dev. Cell 8:937-947(2005) [PubMed: 15935782] [Abstract]
Cited for: INTERACTION WITH BRO1.
[8]"Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body."
Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.
Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006) [PubMed: 16601096] [Abstract]
Cited for: INTERACTION WITH VTA1.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, MASS SPECTROMETRY.
[10]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-119, MASS SPECTROMETRY.
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, MASS SPECTROMETRY.
[12]"Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation."
Teis D., Saksena S., Emr S.D.
Dev. Cell 15:578-589(2008) [PubMed: 18854142] [Abstract]
Cited for: ASSEMBLY OF THE ESCRT-III COMPLEX.
[13]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; THR-116; SER-119; SER-193 AND SER-204, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
PIRS52590.
RefSeqNP_013125.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1747N.
IntActP39929. 18 interactions.
STRINGP39929.

Proteomic databases

PeptideAtlasP39929.

Genome annotation databases

EnsemblYLR025W; YLR025W; YLR025W; Saccharomyces cerevisiae. [Genome view]
GeneID850712.
KEGGsce:YLR025W.
NMPDRfig|4932.3.peg.4116.

Organism-specific databases

CYGDYLR025w.
SGDS000004015. SNF7.

Phylogenomic databases

HOGENOMP39929.
OMAPSAQEAI
OrthoDBEOG96HHTF

Gene expression databases

ArrayExpressP39929.
GenevestigatorP39929.
GermOnlineYLR025W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio966772.

Entry information

Entry nameSNF7_YEAST
AccessionPrimary (citable) accession number: P39929
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 24, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents